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Updated: May 29, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign
Gonzalo de Gonzalo1, Christian Smit, Jianfeng Jin
1Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Abstract:
By cofactor redesign, self-sufficient monooxygenases could be prepared. Tight binding of N-alkylated flavins to riboflavin-binding protein results in the creation of artificial flavoenzymes capable of H(2)O(2)-driven enantioselective sulfoxidations. By altering the flavin structure, opposite enantioselectivities could be achieved, in accordance with the binding mode predicted by in silico flavin-protein docking of the unnatural flavin cofactors. The study shows that cofactor redesign is a viable approach to create artificial flavoenzymes with unprecedented activities.
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